ID   BETA_STAXY              Reviewed;         560 AA.
AC   Q9X2M2;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Oxygen-dependent choline dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00750};
DE            Short=CDH {ECO:0000255|HAMAP-Rule:MF_00750};
DE            Short=CHD {ECO:0000255|HAMAP-Rule:MF_00750};
DE            EC=1.1.99.1 {ECO:0000255|HAMAP-Rule:MF_00750};
DE   AltName: Full=Betaine aldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00750};
DE            Short=BADH {ECO:0000255|HAMAP-Rule:MF_00750};
DE            EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00750};
GN   Name=betA {ECO:0000255|HAMAP-Rule:MF_00750}; Synonyms=cudB;
OS   Staphylococcus xylosus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 20267 / Isolate C2A;
RX   PubMed=10094709; DOI=10.1128/jb.181.7.2273-2278.1999;
RA   Rosenstein R., Futter-Bryniok D., Gotz F.;
RT   "The choline-converting pathway in Staphylococcus xylosus C2A: genetic and
RT   physiological characterization.";
RL   J. Bacteriol. 181:2273-2278(1999).
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC       betaine. Catalyzes the oxidation of choline to betaine aldehyde and
CC       betaine aldehyde to glycine betaine at the same rate.
CC       {ECO:0000255|HAMAP-Rule:MF_00750}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC         ChEBI:CHEBI:17499; EC=1.1.99.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00750};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00750};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00750};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine aldehyde from choline (cytochrome c reductase
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00750}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00750}.
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DR   EMBL; AF009415; AAD23901.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X2M2; -.
DR   SMR; Q9X2M2; -.
DR   STRING; 1288.SXYLSMQ121_0226; -.
DR   eggNOG; COG2303; Bacteria.
DR   UniPathway; UPA00529; UER00385.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_00750; Choline_dehydrogen; 1.
DR   InterPro; IPR011533; BetA.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; PTHR11552; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01810; betA; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..560
FT                   /note="Oxygen-dependent choline dehydrogenase"
FT                   /id="PRO_0000205605"
FT   ACT_SITE        472
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
FT   BINDING         6..35
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
SQ   SEQUENCE   560 AA;  62384 MW;  4D8395EED9E584D7 CRC64;
     MKESYDYIII GGGSAGSVLG GRLSEDVSNN VLVLEAGRSD YPWDLLIQMP AALMYPAGNK
     LYDWIYETTP EPHMDGRKVG HARGKVLGGS SSINGMIYQR GNPMDYEKWA KPEGMESWDY
     AHCLPYFKRL ETTFGSKKGD PYRGHHGPIK LRRGPADNPL FQAFFDAGVE AGYNKTPDVN
     GFRQEGFGPF DSQVHNGRRV SASRAYLHPA MKRKNLEVQT RAFVTKLNFE GNKVTGVTFK
     KNGKEHTESA KEVILSGGAI NSPQLLQLSG IGDSEHLRSL GIEPRIHLPG VGENFEDHLE
     VYVQHACKQP VSMQPSLNKL KMPFIGLQWI LGRKGAAASN HFEGGGFVRS NDDVDYPNLM
     FHFLPIAVRY DGTKAPAAHG YQVHVGPMYS NSRGHLKIKS KDPFEKPEFV FNYLSTEEDK
     REWVEAIKVA RNILKQKALD PFNGGEISPG PEVQTDEEII EWVKRDGETA LHPSCSCRMG
     PASDEMSVVD PETFKVHGME NLRVVDASVM PRTTNGNIHS PVLMMAERAS DIIRGKKPLD
     PQYIDFYRHG VHDKDAGTVK